Purification and Identification of Natural Inhibitors of Protein Arginine Methyltransferases from Plants.

ABSTRACT: Protein arginine methyltransferase (PRMT) enzymes catalyze posttranslational modifications of target proteins and are often upregulated in human cancers. In this study, we purified two chemical compounds from seeds of Foeniculum vulgare based on their ability to inhibit the enzymatic activity of PRMT5. These two compounds were identified as Pheophorbide a (PPBa) and Pheophorbide b (PPBb), two breakdown products of chlorophyll. PPBa and PPBb inhibited the enzymatic activity of both Type I and Type II PRMTs with IC₅₀ values at sub micromole concentrations, inhibited the arginine methylation of histones in cells, and suppressed proliferation of prostate cancer cells. Molecular docking results predicted that PPBa binds to an allosteric site in the PRMT5 structure with a high

SUBMITTER: Wang Z 

PROVIDER: S-EPMC9022574 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature